Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Automatic Gene Ontology annotation based on Rhea mapping
Functional characterization of a novel ArgA from Mycobacterium tuberculosis.
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Rv2747 turns over glutamate and glutamine, with glutamine the better tested acyl acceptor.
"Although l -glutamate and l -glutamine served as substrates for Rv2747"
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Both oligomeric forms were detected by analytical gel filtration.
"the protein existed as a mixture of equal amounts of a dimer and a tetramer."
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The purified enzyme is inhibited by the pathway end product arginine.
"The IC 50 value determined for arginine was 26 ± 3 μM"
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The physiological efficiency problem and a possible protein partner remain unresolved.
"Another reason might be that Rv2747 requires a protein partner for efficient and more selective acetylation of l -glutamate."
UniProtKB O33289 ArgA from Mycobacterium tuberculosis H37Rv
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Curated target function supports glutamate acetylation and identifies glutamine as a better substrate.
"L-glutamine is a significantly better substrate compared to
CC L-glutamate."
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The protein belongs to a broad GNAT acyltransferase family.
"DR PANTHER; PTHR43626; ACYL-COA N-ACYLTRANSFERASE; 1."
Surprising arginine biosynthesis: a reappraisal of the enzymology and evolution of the pathway in microorganisms.
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Mycobacteria provide the short, single-protein NAGS architecture.
"Short NAGSs can be single gene products, as in Mycobacterium spp. and Thermus spp."